Category: Krezel Publications

Dr. Krezel’s Publications

Small Molecule Antagonists of the DNA Repair ERCC1/XPA Protein-Protein Interaction

Robert Obermann, Bereket Yemane, Cassie Jarvis, Francisco M Franco, Yevhenii Kyriukha, William Nolan, Beth Gohara, Andrzej M Krezel, Scott A Wildman & James W Janetka (2024). “Small Molecule Antagonists of the DNA Repair ERCC1/XPA Protein-Protein Interaction” ChemMedChem. 2024 Feb 1:e202300648. doi: 10.1002/cmdc.202300648. Online ahead of print. (Abstract)

Stabilization and structure determination of integral membrane proteins by termini restraining

Shixuan Liu, Shuang Li, Andrzej M. Krezel, & Weikai Li (2022). “Stabilization and structure determination of integral membrane proteins by termini restraining” Nat Protoc. 2022 Jan 17. doi: 10.1038/s41596-021-00656-5. Online ahead of print. (Abstract)

Structural basis of antagonizing the vitamin K catalytic cycle for anticoagulation

Shixuan Liu, Shuang Li, Guomin Shen, Narayanasami Sukumar, Andrzej M. Krezel, & Weikai Li (2021). “Structural basis of antagonizing the vitamin K catalytic cycle for anticoagulation” Science. 2021 Jan 1;371(6524):eabc5667. doi: 10.1126/science.abc5667. Epub 2020 Nov 5. (Abstract)

Atypical Cadherin Dachsous1b Interacts with Ttc28 and Aurora B to Control Microtubule Dynamics in Embryonic Cleavages.

Chen J., Castelvecchi G.D., Li-Villarreal N., Raught B., Krezel A.M., McNeill H., & Solnica-Krezel L. (2018). “Atypical Cadherin Dachsous1b Interacts with Ttc28 and Aurora B to Control Microtubule Dynamics in Embryonic Cleavages.” Dev Cell. 2018 May 7;45(3):376-391.e5. doi: 10.1016/j.devcel.2018.04.009. (Abstract)

MFN2 agonists reverse mitochondrial defects in preclinical models of Charcot-Marie-Tooth disease type 2A.

Rocha A.G., Franco A., Krezel A.M., Rumsey J.M., Alberti J.M., Knight W.C., Biris N., Zacharioudakis E., Janetka J.W., Baloh R.H., Kitsis R.N., Mochly-Rosen D., Townsend R.R., Gavathiotis E., & Dorn G.W. 2nd (2018). “MFN2 agonists reverse mitochondrial defects in preclinical models of Charcot-Marie-Tooth disease type 2A.” Science. 2018 Apr 20;360(6386):336-341. doi: 10.1126/science.aao1785. (Abstract)

Noroviruses Co-opt the Function of Host Proteins VAPA and VAPB for Replication via a Phenylalanine-Phenylalanine-Acidic-Tract-Motif Mimic in Nonstructural Viral Protein NS1/2.

McCune B.T., Tang W., Lu J., Eaglesham J.B., Thorne L., Mayer A.E., Condiff E., Nice T.J., Goodfellow I., Krezel A.M., & Virgin H.W. (2017). “Noroviruses Co-opt the Function of Host Proteins VAPA and VAPB for Replication via a Phenylalanine-Phenylalanine-Acidic-Tract-Motif Mimic in Nonstructural Viral Protein NS1/2.” MBio. 2017 Jul 11;8(4). pii: e00668-17. doi: 10.1128/mBio.00668-17. (Abstract)

Solution NMR structure of CsgE: Structural insights into a chaperone and regulator protein important for functional amyloid formation.

Shu Q., Krezel A.M., Cusumano Z.T., Pinkner J.S., Klein R., Hultgren S.J., & Frieden C. (2016). “Solution NMR structure of CsgE: Structural insights into a chaperone and regulator protein important for functional amyloid formation.” Proc Natl Acad Sci U S A. 2016 Jun 28;113(26):7130-5. doi: 10.1073/pnas.1607222113. Epub 2016 Jun 13. (Abstract)

Genetic Evolution of a Helicobacter pylori Acid-Sensing Histidine Kinase and Gastric Disease.

Krishna U., Romero-Gallo J., Suarez G., Azah A., Krezel A.M., Varga M.G., Forsyth M.H., & Peek R.M. Jr. (2016). “Genetic Evolution of a Helicobacter pylori Acid-Sensing Histidine Kinase and Gastric Disease.” J Infect Dis. 2016 Aug 15;214(4):644-8. doi: 10.1093/infdis/jiw189. Epub 2016 May 10. (Abstract)

Helicobacter pylori RNA polymerase α-subunit C-terminal domain shows features unique to ɛ-proteobacteria and binds NikR/DNA complexes.

Borin B.N., Tang W., & Krezel A.M. (2014). “Helicobacter pylori RNA polymerase α-subunit C-terminal domain shows features unique to ɛ-proteobacteria and binds NikR/DNA complexes.” Protein Sci. 2014 Apr;23(4):454-63. doi: 10.1002/pro.2427. Epub 2014 Feb 4. (Abstract)

Murine norovirus protein NS1/2 aspartate to glutamate mutation, sufficient for persistence, reorients side chain of surface exposed tryptophan within a novel structured domain.

Borin B.N., Tang W., Nice T.J., McCune B.T., Virgin H.W., & Krezel A.M. (2013). “Murine norovirus protein NS1/2 aspartate to glutamate mutation, sufficient for persistence, reorients side chain of surface exposed tryptophan within a novel structured domain.” Proteins. 2014 Jul;82(7):1200-9. doi: 10.1002/prot.24484. Epub 2013 Dec 26. (Abstract)